Enterovirus VP1 capsid protein (VP1)

The Enterovirus VP1 capsid protein is a major structural protein that forms the icosahedral shell of viruses within the Enterovirus genus, including poliovirus, coxsackievirus, and rhinovirus (UniProt P03300). It is the most surface-exposed protein and plays a pivotal role in viral pathogenesis by mediating attachment to host cell receptors and facilitating the entry of the viral genome (PubMed: 25605940). VP1 contains a specialized hydrophobic pocket, often called the "canyon," which is critical for the structural stability and uncoating of the virus (PubMed: 17307109). This protein is a significant target for antiviral therapy, specifically for a class of drugs known as capsid binders, such as pleconaril and pocapavir (PubMed: 11850360, PubMed: 26150541). These inhibitors bind within the VP1 hydrophobic pocket, preventing the conformational changes necessary for the virus to release its RNA into the host cell. Furthermore, VP1 is highly immunodominant and serves as the primary basis for the serological and molecular classification of enterovirus strains (PubMed: 10430872). Mutations within the VP1 protein are frequently associated with the development of drug resistance, posing a challenge for therapeutic development (PubMed: 15105531).

Other names

Viral protein 1Capsid protein VP1VP1 proteinEnterovirus structural protein 1

Capsid binders occupy a hydrophobic pocket in the VP1 protein, which stabilizes the virion and prevents the uncoating and release of viral RNA (PubMed: 17307109). This interaction can also inhibit viral attachment to host receptors by preventing the necessary conformational changes for receptor engagement (PubMed: 11850360).